Research workbench
In vitro assembled tau filaments into quadruple helical filaments type 1 (2C)
Analyse In vitro assembled tau filaments into quadruple helical filaments type 1 (2C) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QJV
- Type
- protein
- Length
- 900 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microtubule-associated protein tau
- UniProt
- P10636
Structure
electron microscopy · 1 distinct chain · 0% helix, 60% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F, B, C, D, E, K, G, H, I, J, L | Microtubule-associated protein tau | protein | 75 | 0% helix, 60% strand | P10636 |
Interfaces
31 interfaces between chains.
- C–E · 3107 Ų buried · 83 hydrogen bonds · protein-protein
- B–D · 3088 Ų buried · 80 hydrogen bonds · protein-protein
- A–D · 3079 Ų buried · 84 hydrogen bonds · protein-protein
- K–J · 3074 Ų buried · 80 hydrogen bonds · protein-protein
- H–J · 3073 Ų buried · 83 hydrogen bonds · protein-protein
Compared structures
- 7QJV · In vitro assembled tau filaments into Quadruple Helical Filaments type 1 (2c) · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P10636
- Elsewhere: RCSB PDB 7QJV · PDBe 7QJV · UniProt P10636
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